S-sulfohemoglobin and disulfide exchange:: The mechanisms of sulfide binding by Riftia pachyptila hemoglobins

被引:73
作者
Zal, F [1 ]
Leize, E
Lallier, FH
Toulmond, A
Van Dorsselaer, A
Childress, JJ
机构
[1] Univ Calif Santa Barbara, Dept Sci Biol, Santa Barbara, CA 93106 USA
[2] Univ Calif Santa Barbara, Inst Marine Sci, Santa Barbara, CA 93106 USA
[3] Univ Strasbourg 1, Inst Chim, Lab Spectrometrie Masse Bioorgan, CNRS URA 31, F-67008 Strasbourg, France
[4] UPMC, Equipe Ecophysiol, CNRS, Inst Natl Sci Univers,Stn Biol, F-29682 Roscoff, France
关键词
D O I
10.1073/pnas.95.15.8997
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The deep sea hydrothermal tube worm Riftia pachyptila possesses a multihemoglobin system with three different extracellular hemoglobins (Hbs; V1, V2, and C1): two dissolved in the vascular blood, V1 and V2, and one in the coelomic fluid, C1. V1 consists of four heme-containing chains and four linker chains. The globin chains making up V2 and C1 are, with one exception, common to V1, Remarkably these Hbs are able to bind oxygen and sulfide simultaneously and reversibly at two different sites. Two of the globin chains found in these three Riftia Hbs possess one free Cys residue and for at least one of the globins, the b-Cys(75) is conserved among vestimentifera (Lamellibrachia sp,) and pogonophora (Oligobrachia mashikoi). By selectively blocking the free Cys with N-ethylmaleimide and using electrospray ionization mass spectrometry experiments, we show that these Cys residues are involved in sulfide binding by Riftia Hbs. Moreover, we also demonstrate that the larger V1 Hb can form persulfide groups on its linker chains, a mechanism that can account for the higher sulfide-binding potential of this Hb.
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页码:8997 / 9002
页数:6
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